Histidine transaminase explained

histidine transaminase
Ec Number:	2.6.1.38
Cas Number:	37277-92-2
Go Code:	0008110

In enzymology, a histidine transaminase is an enzyme that catalyzes the chemical reaction

L-histidine + 2-oxoglutarate

\rightleftharpoons (imidazol-5-yl)pyruvate + L-glutamate

Thus, the two substrates of this enzyme are L-histidine and 2-oxoglutarate, whereas its two products are (imidazol-5-yl)pyruvate and L-glutamate.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-histidine:2-oxoglutarate aminotransferase. Other names in common use include histidine aminotransferase, and histidine-2-oxoglutarate aminotransferase. This enzyme participates in histidine metabolism.

References

• Coote JG, Hassall H . 1969 . The role of imidazol-5-yl-lactate-nicotinamide-adenine dinucleotide phosphate oxidoreductase and histidine-2-oxoglutarate aminotransferase in the degradation of imidazol-5-yl-lactate by Pseudomonas acidovorans . Biochem. J. . 111 . 237 - 9 . 4303364 . 2 . 1187811 .
• Wickremasinghe R, Hedegaard J, Roche J . 1967 . Degradation de la L-histidine chez Escherichia coli B: formation de l'acide imidazolepyruvique par une histidine-transaminase . C. R. Soc. Biol. . 161 . 1891 - 1896 .